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Protoxin II,CAS#:165168-50-3,Catalog Number: N1030-V,Sequence:YCQKWMWTCDSERKCCEGMVCRLWCKKKLW
NaV channels and T-type Ca2+ channels, ProTx-II inhibits NaV channels1. ProTx-II could also modulate T-type Ca2+ channels at higher concentrations.
Protoxin-II is a neurotoxin that is derived from the venom of the Peruvian green velvet tarantula (Thrixopelma pruriens).
ProTx-II is a 30-amino acid peptide with a molecular weight of 3826.65 Da. The structure of ProTx-II is amphipathic, with mostly hydrophobic residues on one face of the toxin. The toxin is formed by an inhibitor cystine knot (ICK) backbone region and a flexible C-terminal tail region.
ProTx-II inhibits several human sodium channel subtypes, ranging from Nav1.1 up to Nav1.8. However, this toxin is, at least, 100-fold more potent against Nav1.7 than other human Nav channel subtypes. At a concentration of 0.3 nM, this toxin blocks Nav1.7 by 50%.
Besides sodium channels, ProTx-II also inhibits some subtypes of voltage-gated calcium channels, Cav1.2 and Cav3.2. From the fact that ProTx-II is able to inhibit several sodium and calcium channel subtypes, we can infer that the toxin-channel interaction surface is conserved between these channels.
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Protoxin II,CAS#:165168-50-3,Catalog Number: N1030-V,Sequence:YCQKWMWTCDSERKCCEGMVCRLWCKKKLW
NaV channels and T-type Ca2+ channels, ProTx-II inhibits NaV channels1. ProTx-II could also modulate T-type Ca2+ channels at higher concentrations.
Protoxin-II is a neurotoxin that is derived from the venom of the Peruvian green velvet tarantula (Thrixopelma pruriens).
ProTx-II is a 30-amino acid peptide with a molecular weight of 3826.65 Da. The structure of ProTx-II is amphipathic, with mostly hydrophobic residues on one face of the toxin. The toxin is formed by an inhibitor cystine knot (ICK) backbone region and a flexible C-terminal tail region.
ProTx-II inhibits several human sodium channel subtypes, ranging from Nav1.1 up to Nav1.8. However, this toxin is, at least, 100-fold more potent against Nav1.7 than other human Nav channel subtypes. At a concentration of 0.3 nM, this toxin blocks Nav1.7 by 50%.
Besides sodium channels, ProTx-II also inhibits some subtypes of voltage-gated calcium channels, Cav1.2 and Cav3.2. From the fact that ProTx-II is able to inhibit several sodium and calcium channel subtypes, we can infer that the toxin-channel interaction surface is conserved between these channels.